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目的：探讨降低鼠源性单克隆抗体（单抗）对人体的免疫原性。方法：应用基因工程技术扩增出SZ－51重链和轻链可变区cDNA与连接肽（Gly4Ser）3的寡核苷酸片段进行拼接构建了表达载体pHEN1-51scFv，并导入大肠杆菌HB2151中进行表达。结果：其表达产物可折叠成可溶性并具有抗原结合能力的单链抗体（scFv，小分子肽）释放到细菌培养上清中。结论：该分泌型小肽抗体能特异地与α－颗粒膜蛋白结合，具有与原鼠源单抗一致的抗原结合特性。
Objective: To investigate the immunogenicity of murine monoclonal antibody (mAb) to human. Methods: The oligonucleotide fragments of SZ-51 heavy chain and light chain variable region cDNA and peptide Gly4Ser 3 were amplified by gene engineering technique to construct the expression vector pHEN1-51scFv and then introduced into E. coli HB2151 Express. Results: Single chain antibody (scFv, small molecule peptide) whose expression product can be folded into a soluble and antigen-binding ability was released into the bacterial culture supernatant. Conclusion: The secretory small peptide antibody can specifically bind to the α-granule membrane protein and has the antigen-binding characteristics consistent with the original murine monoclonal antibody.